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. 2018 Jan 10;8:298. doi: 10.1038/s41598-017-18567-5

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Snapshots from the molecular dynamic trajectories representing the statistically significant hydrogen bonds for the h4_7 (A), h12_15 (B), and r12_15 (C) Aβ tetrapeptides bound at N-ACE substrate tunnel. Panel D shows distorted conformation of r4_7 at the final time step of the molecular dynamic trajectory, where both characteristic hydrogen bonds F4 O - H331 Nε2 Hε2 and N-terminal acetyl O - Y501 OχHχ are observed. Peptide carbon atoms are in green; carbon atoms of receptor residues, important for peptide stabilization, are in cyan; grey sticks depict receptor residues, involved in zinc chelation and catalysis.